122242-30-2Relevant articles and documents
Structure diversification of vancomycin through peptide-catalyzed, site-selective lipidation: A catalysis-based approach to combat glycopeptide-resistant pathogens
Yoganathan, Sabesan,Miller, Scott J.
supporting information, p. 2367 - 2377 (2015/03/30)
The emergence of antibiotic-resistant infections highlights the need for novel antibiotic leads, perhaps with a broader spectrum of activity. Herein, we disclose a semisynthetic, catalytic approach for structure diversification of vancomycin. We have identified three unique peptide catalysts that exhibit site-selectivity for the lipidation of the aliphatic hydroxyls on vancomycin, generating three new derivatives 9a, 9b, and 9c. Incorporation of lipid chains into the vancomycin scaffold provides promising improvement of its bioactivity against vancomycin-resistant enterococci (Van A and Van B phenotypes of VRE). The MICs for 9a, 9b, and 9c against MRSA and VRE (Van B phenotype) range from 0.12 to 0.25 μg/mL. We have also performed a structure-activity relationship (SAR) study to investigate the effect of lipid chain length at the newly accessible G4-OH derivatization site.
Antibiotic activities and affinities for bacterial cell wall analogue of N-demethylvancomycin and its derivatives
Yan, Husheng,Qi, Dongfeng,Cheng, Xiaohui,Song, Zhengji,Li, Wenlan,He, Binglin
, p. 750 - 756 (2007/10/03)
N-Demethylvancomycin, which has been clinically used in China, is one member of vancomycin group (glycopeptide) antibiotics. It differs from vancomycin only in that methyl group on the amino group of the N-terminal residue of vancomycin has been replaced